Glutamate dehydrogenase from Pantoea ananatis: A new bacterial enzyme with dual coenzyme specificity.

ABSTRACT: Glutamate dehydrogenase (GDH) catalyzes the reversible conversion of α-ketoglutarate (α-KG) to L-glutamate (Glu) and plays an important role in linking nitrogen and carbon metabolism. However, little is known about this enzyme in the biotechnologically important bacterium Pantoea ananatis. In this study, we report for the first time the enzymatic characteristics of the P. ananatis AJ13355 GDH, GdhPa. GdhPa, a 46.5 kDa protein of the GDH50s group, was expressed in Escherichia coli host, purified, and biochemically characterized. In vitro enzymatic activity assays revealed that GdhPa is capable of catalyzing both the reductive amination of α-KG and the oxidative deamination of Glu with dual coenzyme specificity (NAD(H)/NADP(H)), a rare occurrence in bacterial GDHs. The NADH and NADPH specifi

SUBMITTER: Kharchenko MS 

PROVIDER: S-EPMC12364357 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature